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Conserved domains on  [gi|1352739990|gb|AVI83333|]
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glucose-1-phosphate thymidylyltransferase [Pseudomonas syringae pv. tomato]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

sugar nucleotidyltransferase such as glucose-1-phosphate thymidylyltransferase, which catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis

CATH:  3.90.550.10
EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0046872|GO:0000271
PubMed:  9445404|12691742
SCOP:  4000694

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-292 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 567.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1352739990 246 EQRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLLD 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-292 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 567.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1352739990 246 EQRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLLD 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 7-291 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQP 86
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  87 TPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEKP 166
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 167 AAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTIE 246
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1352739990 247 QRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLL 291
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-245 2.40e-179

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 494.02  E-value: 2.40e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-291 4.25e-150

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 422.16  E-value: 4.25e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:PRK15480    4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:PRK15480   84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:PRK15480  164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1352739990 246 EQRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLL 291
Cdd:PRK15480  244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-243 5.33e-100

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 293.01  E-value: 5.33e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPC-CLILGDNIFYGQHFSDNLRSA--SQQTEGATVFGYHVSDPERFGVVEFDETGRALSI 162
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHieKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 163 EEKPAAPK-SSYAVTGLYFYDNQVVE-IAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASH 240
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 1352739990 241 FVH 243
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-292 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 567.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1352739990 246 EQRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLLD 292
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLD 287
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 7-291 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQP 86
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  87 TPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEKP 166
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 167 AAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTIE 246
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1352739990 247 QRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLL 291
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-245 2.40e-179

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 494.02  E-value: 2.40e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-291 4.25e-150

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 422.16  E-value: 4.25e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:PRK15480    4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEK 165
Cdd:PRK15480   84 PSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 166 PAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASHFVHTI 245
Cdd:PRK15480  164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1352739990 246 EQRQGWKVACLEEIAYTNGWITAAQLGEQAQKLKKTGYGQYLQKLL 291
Cdd:PRK15480  244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-243 5.33e-100

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 293.01  E-value: 5.33e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQ 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIGEDPC-CLILGDNIFYGQHFSDNLRSA--SQQTEGATVFGYHVSDPERFGVVEFDETGRALSI 162
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHieKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 163 EEKPAAPK-SSYAVTGLYFYDNQVVE-IAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGFAWLDTGTHESLLEASH 240
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 1352739990 241 FVH 243
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 7-242 3.49e-69

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 214.35  E-value: 3.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLII--STPEDlpsFRKLLGDGSQYGIELTYAE 84
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEE---IKEALGDGSRFGVRITYIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  85 QPTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQhFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDEtGRALSIEE 164
Cdd:cd04189    79 QEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG-ISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD-GRIVRLVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352739990 165 KPAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQ-KSLTVEILgRGFaWLDTGTHESLLEASHFV 242
Cdd:cd04189   157 KPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRgRRVGYSIV-TGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-230 2.49e-61

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 193.57  E-value: 2.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDlPSFRKLLGDGSQYGIELTYAEQPT 87
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  88 PDGLAQAFIIGEEFIGEDPCCLILGDNIFYGqHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEKPA 167
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352739990 168 APKSSYAVTGLYFYDNQVVEIAKSIKPseRGELEITDVNRAYLEQKSLTVeILGRGFaWLDTG 230
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 7-238 2.86e-59

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 193.00  E-value: 2.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLLGDGSQYGIELTYAEQP 86
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  87 TPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGqHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIEEKP 166
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352739990 167 AAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRaYLEQKSLTVEILGRGFAWLDTGTHESLLEA 238
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQ-WLIEKGYKVGGSKVTGWWKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 7-239 1.30e-46

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 160.84  E-value: 1.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDlPSFRKLLGDGSQYGIELTYAEQP 86
Cdd:TIGR03992   2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  87 TPDGLAQAFIIGEEFIgEDPCCLILGDNIFYGQHFSDNLRsasqqTEGATVFGYHVSDPERFGVVEFDEtGRALSIEEKP 166
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLIR-----AEAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEKP 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352739990 167 AAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGRGfaWLDTGTHESLLEAS 239
Cdd:TIGR03992 154 ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-238 2.35e-45

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 153.38  E-value: 2.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVlIIST---PEDlpsFRKLLGDGSQYGIELTYA 83
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVgylAEQ---IEEYFGDGSRFGVRITYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  84 EQPTP----DGLAQAfiigEEFIGEDPCCLILGDnIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRA 159
Cdd:COG1208    77 DEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352739990 160 LSIEEKPAAPKSSYAVTGLYFYDNQVVEiakSIKPSERgeLEITDVNRAYLEQKSLTVEILgRGFaWLDTGTHESLLEA 238
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFD---YIPEGEP--FDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-239 2.12e-28

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 109.93  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTP-----EDL--PSF---RKLLGDGSQ 75
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiEDHfdRSYeleETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  76 ----------YGIELTYAEQPTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQHF-SDNLRSASQQTeGATVFGYHVSD 144
Cdd:cd02541    81 dlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEKT-GASVIAVEEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 145 PE---RFGVVEF----DETGRALSIEEKPA---APkSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKS 214
Cdd:cd02541   160 PEdvsKYGIVKGekidGDVFKVKGLVEKPKpeeAP-SNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238

                         250       260
                  ....*....|....*....|....*.
gi 1352739990 215 -LTVEILGRgfaWLDTGTHESLLEAS 239
Cdd:cd02541   239 vYAYVFEGK---RYDCGNKLGYLKAT 261
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 9-238 1.71e-22

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 92.96  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVlIIST---PEDLPSFrklLGDGSQYGIELTYAEQ 85
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAEMIEDY---FGDGSKFGVNISYVRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  86 PTPDGLAQAFIIGEEFIgEDPCCLILGDnIFYGQHFSDNLRSASQQTEGATVFG--YHVSDPerFGVVEFDEtGRALSIE 163
Cdd:cd06426    78 DKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETEG-GRITSIE 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352739990 164 EKpaaPKSSYAV-TGLYFYDNQVVEiakSIKPSERgeLEITDVNRAYLEQKSLTV--EILGRgfaWLDTGTHESLLEA 238
Cdd:cd06426   153 EK---PTHSFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKKVGvfPIHEY---WLDIGRPEDYEKA 219
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 6-238 2.04e-22

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 93.57  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIIS-----TPEDlpSF-------RKLLGDG 73
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTgrgkrAIED--HFdysyeleHQLEKRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  74 SQYGIE----------LTYAEQPTPDGLAQAFIIGEEFIGEDPCCLILGDNIFygQHFSDNLRSASQQTE--GATVFGYH 141
Cdd:TIGR01099  79 KEELLEevrkisnlatIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIV--VNEEPALKQMIKAYEktGCSIIAVQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 142 VSDPE---RFGVVEF----DETGRALSIEEKPA---APkSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLE 211
Cdd:TIGR01099 157 EVPKEevsKYGVIDGegieKDLYKVKNMVEKPKpeeAP-SNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLE 235

                         250       260
                  ....*....|....*....|....*...
gi 1352739990 212 QKS-LTVEILGRGFawlDTGTHESLLEA 238
Cdd:TIGR01099 236 NETvLAYKFNGKRY---DCGSKLGYLEA 260
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 7-240 4.72e-21

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 89.19  E-value: 4.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREV-LIIS-TPEDLPSFRKLLGDgsQYGIELTYAE 84
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIiLAVNyRPEDMVPFLKEYEK--KLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  85 QPTPDGLAQAFIIGEEFIGEDP-CCLILGDNIFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDE-TGRALSI 162
Cdd:cd06425    80 ETEPLGTAGPLALARDLLGDDDePFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDEnTGRIERF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 163 EEKPAAPKSSYAVTGLYFYDNQV--------VEIAKSIKP--SERGELEITDVNrayleqksltveilgrGFaWLDTGTH 232
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVldriplrpTSIEKEIFPkmASEGQLYAYELP----------------GF-WMDIGQP 222


                  ....*...
gi 1352739990 233 ESLLEASH 240
Cdd:cd06425   223 KDFLKGMS 230
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-238 4.23e-20

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 87.78  E-value: 4.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   6 RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYplSV--LMLAGMREVLIISTP-----ED-------LPSF----- 66
Cdd:COG1210     4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiEDhfdrsyeLEATleakg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  67 -RKLLG--DGSQYGIELTYAEQPTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQhfSDNLR---SASQQTEGATVFGY 140
Cdd:COG1210    82 kEELLEevRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKqmiEVYEETGGSVIAVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 141 HVSDPE--RFGVVEFDET-GRALSIE---EKPA---APkSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYL- 210
Cdd:COG1210   160 EVPPEEvsKYGIVDGEEIeGGVYRVTglvEKPApeeAP-SNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAk 238

                         250       260
                  ....*....|....*....|....*...
gi 1352739990 211 EQKSLTVEILGRgfaWLDTGTHESLLEA 238
Cdd:COG1210   239 EEPVYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 9-238 5.08e-20

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 86.07  E-value: 5.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVlIISTpedlpSFRK-----LLGDGSQYGIELTYA 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSV-----GYLAeqieeYFGDGYRGGIRIYYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  84 EQPTPDGLAQAFIIGEEFIGEDPCCLILGDNIFYGQhFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSIE 163
Cdd:cd06915    76 IEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352739990 164 EKPAAPKSSYAVTGLYFYDNQVVEIAKSIKPSergeLEiTDVNRAYLEQKSLtveilgRGFA----WLDTGTHESLLEA 238
Cdd:cd06915   155 EKGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-238 7.42e-16

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 74.91  E-value: 7.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVlIIST---PEDLPSFrklLGDgSQYGIELTYA 83
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlADQIEAH---LGD-SRFGLRITIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  84 EQP-----TPDGLAQAfiigEEFIGEDPCCLILGDnIFYGQHFSDNLRSASQQTEG--ATVFGYHVSDPERFGVVEFDET 156
Cdd:cd06422    76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDAllLLLPLVRNPGHNGVGDFSLDAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 157 GRALSIEEKPAAPkssYAVTGLYFYDNQVVEiakSIKPserGELEITDVNRAYLEQKSLTVEILgRGFaWLDTGTHESLL 236
Cdd:cd06422   151 GRLRRGGGGAVAP---FTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLL 219


                  ..
gi 1352739990 237 EA 238
Cdd:cd06422   220 AA 221
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-70 4.75e-14

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 69.61  E-value: 4.75e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLPSFRKLL 70
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
1-218 1.89e-13

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 69.16  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   1 MTTIN---RKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIIS------------TPEDLPS 65
Cdd:PRK13389    1 MAAINtkvKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  66 F------RKLLGDGSQY---GIELTYAEQPTPDGLAQAFIIGEEFIGEDPCCLILGDNIF--YGQHFS-DNLRSASQ--- 130
Cdd:PRK13389   81 MlekrvkRQLLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSqDNLAEMIRrfd 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 131 QTEGATVFGYHVSDPERFGVVEFD-------ETGRALSIEEKPAAPK--SSYAVTGLYFYDNQVVEIAKSIKPSERGELE 201
Cdd:PRK13389  161 ETGHSQIMVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQ 240

                         250
                  ....*....|....*..
gi 1352739990 202 ITDVNRAYLEQKslTVE 218
Cdd:PRK13389  241 LTDAIDMLIEKE--TVE 255
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 8-182 2.62e-13

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 69.33  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPI---Y---DkpmiFyPLSVLMLAGMREVLIIsTPEdlpSFRKL---LGDGSQY-- 76
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFggkYriiD----F-PLSNCVNSGIRRVGVL-TQY---KSHSLndhIGSGKPWdl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  77 -----GIE-LTYAEQPTPD----GLAQAF-----II---GEEFIgedpccLIL-GDNIF---YGQHFSDNLRSasqqteG 134
Cdd:COG0448    75 drkrgGVFiLPPYQQREGEdwyqGTADAVyqnldFIersDPDYV------LILsGDHIYkmdYRQMLDFHIES------G 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352739990 135 A--TVFGYHVSDPE--RFGVVEFDETGRALSIEEKPAAPKSSYAVTGLYFYD 182
Cdd:COG0448   143 AdiTVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
4-204 1.41e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 66.84  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   4 INRKGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIIS------------TPEDLPSF----- 66
Cdd:PRK10122    2 TNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  67 -RKLLGDGSQY---GIELTYAEQPTPDGLAQAFIIGEEFIGEDPCCLILGDnIFYGQHFSDNLR-------SASQQTEGA 135
Cdd:PRK10122   82 kRQLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLRynlaamiARFNETGRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 136 TVFGYHVS-DPERFGVVEFDET-------GRALSIEEKPAAPK---SSYAVTGLYFYDNQVVEIAKSIKPSERGELEITD 204
Cdd:PRK10122  161 QVLAKRMPgDLSEYSVIQTKEPldregkvSRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 7-62 5.07e-11

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 61.12  E-value: 5.07e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPED 62
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHS 57
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 8-218 5.83e-10

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 58.42  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGG--SGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVL-MLAGMREVLIISTPEDLPsFRKLLGDGSQ-YGIELTYA 83
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  84 EQPTPDGLA---------------QAFIIgeefIGEDPCC-LILGDNI-FYGQHFSDNL---RSASQQTegATVFGYHVS 143
Cdd:cd06428    80 QEYKPLGTAgglyhfrdqilagnpSAFFV----LNADVCCdFPLQELLeFHKKHGASGTilgTEASREQ--ASNYGCIVE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352739990 144 DPerfgvvefdETGRALSIEEKPAAPKSSYAVTGLYFYDNQVVEIAKSIKPSERGELEITDVNRAYLEQKSLTVE 218
Cdd:cd06428   154 DP---------STGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 9-238 5.77e-09

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 55.32  E-value: 5.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTP-EDLpsFRKLLGDgsQYGIELTYAEQPT 87
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYkKEQ--IEELLKK--YPNIKFVYNPDYA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  88 PDGLAQAFIIGEEFIGEDpCCLILGDNIFYGQHFsDNLRSASqQTEGATVFGYHVSDPERFGVVEFDETGRaLSIEEKPA 167
Cdd:cd02523    78 ETNNIYSLYLARDFLDED-FLLLEGDVVFDPSIL-ERLLSSP-ADNAILVDKKTKEWEDEYVKDLDDAGVL-LGIISKAK 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352739990 168 APKSSYAVT-GLYFYDNQ----VVEIAKSIKPSERGELEITDVNRAYLEQKSLTVEILGrGFAWLDTGTHESLLEA 238
Cdd:cd02523   154 NLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-57 1.01e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.86  E-value: 1.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352739990   7 KGIILAGGSGTRLHPLTLGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLII 57
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-72 1.77e-07

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 50.90  E-value: 1.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352739990   9 IILAGGSGTRLHpltLGVSKQMLPIYDKPMIFYPLSVLMLAG-MREVLIISTPEDLPSFRKLLGD 72
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 8-239 7.41e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 49.87  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREVLIISTPEDLpSFRKLLGDGSQYGIE-----LT 81
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPL-ELNNHIGIGSPWDLDringgVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  82 ----YAEQPTPD---GLAQAFIIGEEFIGE-DP-CCLIL-GDNIfYGQHFSDNLRSASQQTEGATVFGYHVSDPE--RFG 149
Cdd:PRK05293   85 ilppYSESEGGKwykGTAHAIYQNIDYIDQyDPeYVLILsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVPWEEasRFG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990 150 VVEFDETGRALSIEEKPAAPKSSYAVTGLYFYDNQV-----VEIAKSIKPSER-GEleitDVNRAYLEQKSLTVEILGRG 223
Cdd:PRK05293  164 IMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRlkeylIEDEKNPNSSHDfGK----NVIPLYLEEGEKLYAYPFKG 239

                         250
                  ....*....|....*.
gi 1352739990 224 FaWLDTGTHESLLEAS 239
Cdd:PRK05293  240 Y-WKDVGTIESLWEAN 254
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 9-81 1.01e-06

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 48.67  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352739990   9 IILAGGSGTRLHpltLGVSKQMLPIYDKPMIFYPLSVLM-LAGMREVLIISTPEDLPSFRKLLGDGSQYGIELT 81
Cdd:cd02516     4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIV 74
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-137 1.79e-06

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 46.80  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRlhpltLGVSKQMLPIYDKPMIFYPLSVLMLAGmREVLIISTPEDLPSFRKLLGdgsqygieLTYAEQPT 87
Cdd:pfam12804   1 AVILAGGRSSR-----MGGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1352739990  88 PD-----GLAQAFiigEEFIGEDPCCLILGDNIFYGQHFSDNLRSASQQTEGATV 137
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 8-58 2.79e-06

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 47.15  E-value: 2.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPI---YDkpMIFYPLSVLMLAGMREVLIIS 58
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 9-182 3.53e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 47.91  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTRLHPLTLGVSKQMLPIYDKPMIF-YPLSVLMLAGMREVLIIST-----------------PEDLPSFRKLL 70
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKFRIIdFALSNCINSGIRRIGVLTQykahslirhiqrgwsffREELGEFVDLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  71 GDGSQYGIELTYaeQPTPDGLAQAF-II---GEEFIgedpccLIL-GDNIF---YGQHFSDNLRSasqqteGA--TVFGY 140
Cdd:PRK00725   99 PAQQRVDEENWY--RGTADAVYQNLdIIrryDPKYV------VILaGDHIYkmdYSRMLADHVES------GAdcTVACL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352739990 141 HVSDPE--RFGVVEFDETGRALSIEEKPAAPKS-------SYAVTGLYFYD 182
Cdd:PRK00725  165 EVPREEasAFGVMAVDENDRITAFVEKPANPPAmpgdpdkSLASMGIYVFN 215
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 9-205 3.86e-06

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 47.12  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTR--------LHPLtLGvskqmlpiydKPMIFYPL-SVLMLAGMREVLIISTPEDLpsFRKLLGDGSqygie 79
Cdd:cd02540     2 VILAAGKGTRmksdlpkvLHPL-AG----------KPMLEHVLdAARALGPDRIVVVVGHGAEQ--VKKALANPN----- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  80 LTYAEQPTPDGLAQAFIIGEEFIgEDPCCLILgdnIFYG----------QHFSDNLRSASqqtEGATVFGYHVSDPERFG 149
Cdd:cd02540    64 VEFVLQEEQLGTGHAVKQALPAL-KDFEGDVL---VLYGdvplitpetlQRLLEAHREAG---ADVTVLTAELEDPTGYG 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352739990 150 VVEFDETGRALSI-EEKPAAP---KSSYAVTGLYFYDNQVVEIA-KSIKPS-ERGELEITDV 205
Cdd:cd02540   137 RIIRDGNGKVLRIvEEKDATEeekAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
9-70 6.73e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.28  E-value: 6.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352739990   9 IILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAG-MREVLIISTPEDLPSFRKLL 70
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-205 9.09e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 46.68  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   7 KGIILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDLpsFRKLLGDgsqyGIELTYAEQP 86
Cdd:PRK14357    2 RALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEAEL--VKKLLPE----WVKIFLQEEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  87 TpdGLAQAFIIGEEFIGEDPCCLIL-GDNIFYGQHFSDNL-RSASQQTEGATVFGYHVSDPERFGVVEFDEtGRALSIEE 164
Cdd:PRK14357   73 L--GTAHAVMCARDFIEPGDDLLILyGDVPLISENTLKRLiEEHNRKGADVTILVADLEDPTGYGRIIRDG-GKYRIVED 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1352739990 165 KPAAPKSSYAV---TGLYFYD-NQVVEIAKSIKP-SERGELEITDV 205
Cdd:PRK14357  150 KDAPEEEKKIKeinTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA 195
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-113 2.81e-05

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.00  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLhpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIIsTPEDLPSFRKLLgdgSQYGIELTYAEQPt 87
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV-LGADAEEVAAAL---AGLGVRVVVNPDW- 75

                          90       100
                  ....*....|....*....|....*...
gi 1352739990  88 PDGLAQAFIIGEEFIGE--DPCCLILGD 113
Cdd:COG2068    76 EEGMSSSLRAGLAALPAdaDAVLVLLGD 103
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-113 6.27e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 42.93  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLhpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDlPSFRKLLgdgSQYGIELTYAEQPT 87
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEA-DAVRAAL---AGLPVVVVINPDWE 73

                          90       100
                  ....*....|....*....|....*...
gi 1352739990  88 pDGLAQAFIIGEEFIGED-PCCLI-LGD 113
Cdd:cd04182    74 -EGMSSSLAAGLEALPADaDAVLIlLAD 100
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-170 8.79e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.58  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   9 IILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAGM-REVLIISTPEDlpSFRKLLGDGSQYGIELTYAEQPT 87
Cdd:PRK14355    7 IILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAgRIVLVVGHQAE--KVREHFAGDGDVSFALQEEQLGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  88 PDGLAQAFIIGEEFIGEdpcCLIL-GDN-IFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETGRALSI-EE 164
Cdd:PRK14355   82 GHAVACAAPALDGFSGT---VLILcGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEE 158


                  ....*.
gi 1352739990 165 KPAAPK 170
Cdd:PRK14355  159 KDATPE 164
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 11-83 2.00e-04

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 41.41  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  11 LAGGSGTRLHpltlGVSKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTPEDlPSFRKLL---------GDGSQYGIELT 81
Cdd:COG2266     1 MAGGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNT-PKTREYLkergvevieTPGEGYVEDLN 75


                  ..
gi 1352739990  82 YA 83
Cdd:COG2266    76 EA 77
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 8-185 3.77e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 41.74  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLP---IYDkpMIFYPLSVLMLAGMREVLI------------ISTPEDLPSfrkLLGd 72
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhISQTWRLSG---LLG- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  73 gsQYgIELTYAEQP--------TPDGLAQAFIIGEEfigEDP--CCLILGDNIfYGQHFSDNLRSASQQTEGATVFGYHV 142
Cdd:PRK00844   82 --NY-ITPVPAQQRlgkrwylgSADAIYQSLNLIED---EDPdyVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAAIRV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352739990 143 --SDPERFGVVEFDETGRALSIEEKPAAPKS-------SYAVTGLYFYDNQV 185
Cdd:PRK00844  155 prEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDA 206
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-205 8.67e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   5 NRKGIILAGGSGTRL---HPltlgvsKQMLPIYDKPMIFYPLSVLMLAGMRE-VLIISTPEDLpsFRKLLGDGSQYGIEl 80
Cdd:PRK14354    2 NRYAIILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKiVTVVGHGAEE--VKEVLGDRSEFALQ- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  81 tyAEQPtpdGLAQAFIIGEEFI-GEDPCCLIL-GDN-IFYGQHFSDNLRSASQQTEGATVFGYHVSDPERFGVVEFDETG 157
Cdd:PRK14354   73 --EEQL---GTGHAVMQAEEFLaDKEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENG 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1352739990 158 RALSI-EEKPAAPKSSyAV----TGLYFYDNQV-VEIAKSIKP-SERGELEITDV 205
Cdd:PRK14354  148 EVEKIvEQKDATEEEK-QIkeinTGTYCFDNKAlFEALKKISNdNAQGEYYLTDV 201
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 8-38 8.90e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.61  E-value: 8.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPI---Y---DKPM 38
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYrliDIPM 42
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 8-168 1.07e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.25  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLHPLTLGVSKQMLPIYDK-PMIFYPLSVLMLAGMREVLI------------ISTPEDLPSFrkllgdgS 74
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVltqfnsaslnrhISQTYNFDGF-------S 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990  75 QYGIELTYAEQpTPD------GLAQA-----FIIGEEFIGEdpcCLIL-GDNIfYGQHFSDNLRsASQQTeGA--TVFGY 140
Cdd:PRK02862   79 GGFVEVLAAQQ-TPEnpswfqGTADAvrkylWHFQEWDVDE---YLILsGDQL-YRMDYRLFVQ-HHRET-GAdiTLAVL 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1352739990 141 HVS--DPERFGVVEFDETGRALSIEEKPAA 168
Cdd:PRK02862  152 PVDekDASGFGLMKTDDDGRITEFSEKPKG 181
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-62 1.10e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.02  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352739990   1 MTTiNRKGIILAGGSGTRlhpltLGVSKQMLPIYDKPMIFYPLSVlmLAGMREVLIISTPED 62
Cdd:COG0746     1 MTM-PITGVILAGGRSRR-----MGQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 9-72 1.31e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 39.83  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352739990   9 IILAGGSGTRLhplTLGVSKQMLPIYDKPMIFYPLSVLMLAG-MREVLIISTPEDLPSFRKLLGD 72
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 8-116 1.60e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.86  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352739990   8 GIILAGGSGTRLhPLtlgvsKQMLPIYDKPMIFYPLSVLMLAGMREVLIISTpeDLPSFRKLLgdgSQYGIELTYAEQPT 87
Cdd:pfam02348   2 AIIPARLGSKRL-PG-----KNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVA---KEFGAGVVMTSGSL 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1352739990  88 PDGLAQAFIIGEEFIGEDPC--CLILGDNIF 116
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNDHDDiiVNIQGDNPL 101
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 7-69 2.02e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 38.63  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352739990   7 KGIILAGGSGTRLHpltlGVSKQMLPIYDKPMIFYplsVLM-LAGMREVLIISTPEDLPSFRKL 69
Cdd:PRK00317    5 TGVILAGGRSRRMG----GVDKGLQELNGKPLIQH---VIErLAPQVDEIVINANRNLARYAAF 61
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
5-39 3.50e-03

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.51  E-value: 3.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1352739990   5 NRKGIILAGGSGTRLHPLtlgvS-----KQMLPIY-DKPMI 39
Cdd:COG0836     2 MIYPVILAGGSGTRLWPL----SresypKQFLPLLgEKSLL 38
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 7-39 4.27e-03

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 37.94  E-value: 4.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1352739990   7 KGIILAGGSGTRLHPLtlgvS-----KQMLPIY-DKPMI 39
Cdd:cd02509     2 YPVILAGGSGTRLWPL----SresypKQFLKLFgDKSLL 36
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 9-74 5.31e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 37.43  E-value: 5.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352739990   9 IILAGGSGTRLHPltlGVSKQMLPIYDKPMIFYPLSVLMLAGMRE-VLIISTPEDLPSFRKLLGDGS 74
Cdd:pfam01128   2 VIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPVVDrIVVAVSPDDTPEFRQLLGDPS 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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